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UniProtKB/Swiss-Prot entry P70280


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VAMP7_MOUSE
Primary accession number P70280
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 67)
Name and origin of the protein
Protein name Vesicle-associated membrane protein 7
Synonyms VAMP-7
Synaptobrevin-like protein 1
Gene name
Name: Vamp7
Synonyms: Sybl1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/hmg/6.11.1917; PubMed=9302271 [NCBI, ExPASy, EBI, Israel, Japan]
D'Esposito M., Matarazzo M.R., Ciccodicola A., Strazzullo M., Mazzarella R., Quaderi N.A., Fujiwara H., Ko M.S., Rowe L.B., Ricco A., Archidiacono N., Rocchi M., Schlessinger D., D'Urso M.;
"Differential expression pattern of XqPAR-linked genes SYBL1 and IL9R correlates with the structure and evolution of the region.";
Hum. Mol. Genet. 6:1917-1923(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
DOI=10.1016/S0378-1119(99)00375-3; PubMed=10564831 [NCBI, ExPASy, EBI, Israel, Japan]
Matarazzo M.R., Cuccurese M., Strazzullo M., Vacca M., Curci A., Miano M.G., Cocchia M., Mercadante G., Torino A., D'Urso M., Ciccodicola A., D'Esposito M.;
"Human and mouse SYBL1 gene structure and expression.";
Gene 240:233-238(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Embryo, Kidney, Spleen, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1038/sj.emboj.7600427; PubMed=15470500 [NCBI, ExPASy, EBI, Israel, Japan]
Braun V., Fraisier V., Raposo G., Hurbain I., Sibarita J.-B., Chavrier P., Galli T., Niedergang F.;
"TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles in macrophages.";
EMBO J. 23:4166-4176(2004).
Comments
  • FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.
  • SUBUNIT: Component of the SNARE complex composed of Stx4, Snap23 and Vamp7 that binds Syt7 during lysosomal exocytosis. Component of the SNARE complex composed of Stx7, Stx8, Vamp7 and Vti1b that is required for heterotypic fusion of late endosomes with lysosomes in liver cells (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein (By similarity). Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein (By similarity). Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein.
  • MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) displays impaired receptor-mediated phagocytosis.
  • SIMILARITY: Belongs to the synaptobrevin family.
  • SIMILARITY: Contains 1 longin domain.
  • SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X96737; CAA65509.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133536; CAB94231.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133537; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133538; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133539; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133540; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133541; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ133542; CAB94231.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002825; BAB22386.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011510; BAB27667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK089035; BAC40712.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK165299; BAE38126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003764; AAH03764.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00137647; -.
RefSeq NP_035645.1; -.
UniGene Mm.1517
3D structure databases
HSSP Q9WUF4; 1GL2. [HSSP ENTRY / PDB]
SMR P70280; 1-122.
ModBase P70280.
PTM databases
PhosphoSite P70280; -.
Organism-specific databases
MGI MGI:1096399; Vamp7.
Gene expression databases
ArrayExpress P70280; -.
Bgee P70280; -.
CleanEx MM_VAMP7; -.
Ontologies
GO
GO:0045177; Cellular component: apical part of cell (inferred from direct assay from MGI).
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005794; Cellular component: Golgi apparatus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031902; Cellular component: late endosome membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005765; Cellular component: lysosomal membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0030670; Cellular component: phagocytic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030667; Cellular component: secretory granule membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031201; Cellular component: SNARE complex (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0017156; Biological process: calcium ion-dependent exocytosis (inferred from sequence or structural similarity from UniProtKB).
GO:0008333; Biological process: endosome to lysosome transport (inferred from sequence or structural similarity from UniProtKB).
GO:0043308; Biological process: eosinophil degranulation (inferred from sequence or structural similarity from UniProtKB).
GO:0006888; Biological process: ER to Golgi vesicle-mediated transport (inferred from sequence or structural similarity from UniProtKB).
GO:0043312; Biological process: neutrophil degranulation (inferred from sequence or structural similarity from UniProtKB).
GO:0006911; Biological process: phagocytosis, engulfment (inferred from sequence or structural similarity from UniProtKB).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006906; Biological process: vesicle fusion (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR010908; Longin.
IPR001388; Synaptobrevin.
Graphical view of domain structure.
Pfam PF00957; Synaptobrevin; 1.
Pfam graphical view of domain structure.
PRINTS PR00219; SYNAPTOBREVN.
ProDom PD001229; Synaptobrevin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS50859; LONGIN; 1.
PS00417; SYNAPTOBREVIN; 1.
PS50892; V_SNARE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P70280; -.
Genome annotation databases
Ensembl ENSMUSG00000051412; Mus musculus. [Contig view]
GeneID 20955; -.
KEGG mmu:20955; -.
Phylogenomic databases
HOGENOM P70280; -.
HOVERGEN P70280; -.
OMA P70280; FLCMAND.
Other
NextBio 299904; -.
SOURCE Vamp7; Mus musculus.
ProtoNet P70280.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Coiled coil; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Exocytosis; Golgi apparatus; Lysosome; Membrane; Protein transport; Signal-anchor; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   220  219     Vesicle-associated membrane protein 7. PRO_0000316087
TOPO_DOM   2   188  187     Cytoplasmic (Potential). 
TRANSMEM   189   209  21     Anchor for type IV membrane protein (Potential). 
TOPO_DOM   210   220  11     Vesicular (Potential). 
DOMAIN   7   110  104     Longin. 
DOMAIN   125   185  61     v-SNARE coiled-coil homology. 
COMPBIAS   191   195  5     Poly-Ile. 
MOD_RES   2     2        N-acetylalanine (By similarity). 
Sequence information
Length: 220 AA [This is the length of the unprocessed precursor] Molecular weight: 24967 Da [This is the MW of the unprocessed precursor] CRC64: 109DBA4BE5772B0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI 

        70         80         90        100        110        120 
VYLCITDDDF ERSRAFSFLN EVKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN 

       130        140        150        160        170        180 
KSLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR 

       190        200        210        220 
AMCMKNIKLT IIIIIVSIVF IYIIVSLLCG GFTWPNCVKK 

P70280 in FASTA format

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